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Q86W56 (PARG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly(ADP-ribose) glycohydrolase

EC=3.2.1.143
Gene names
Name:PARG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length976 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. PARG acts both as an endo- and exoglycosidase, releasing PAR of different length as well as ADP-ribose monomers. Required for retinoid acid-dependent gene transactivation, probably by dePARsylating histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters. Ref.17

Catalytic activity

Hydrolyzes poly(ADP-D-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-D-ribose. Ref.5

Subunit structure

Interacts with PCNA. Ref.15

Subcellular location

Isoform 1: Nucleus. Note: Colocalizes with PCNA at replication foci. Relocalizes to the cytoplasm in response to DNA damage. Ref.4 Ref.5 Ref.8 Ref.15

Isoform 2: Cytoplasm. Note: Translocates to the nucleus in response to DNA damage. Ref.4 Ref.5 Ref.8 Ref.15

Isoform 3: Cytoplasm Ref.4 Ref.5 Ref.8 Ref.15.

Isoform 4: Cytoplasm. Mitochondrion Ref.4 Ref.5 Ref.8 Ref.15.

Isoform 5: Mitochondrion matrix Ref.4 Ref.5 Ref.8 Ref.15.

Tissue specificity

Ubiquitously expressed. Ref.1

Domain

The PIP-box mediates interaction with PCNA and localization to replication foci.

Sequence similarities

Belongs to the poly(ADP-ribose) glycohydrolase family.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86W56-1)

Also known as: hPARG111;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q86W56-2)

Also known as: hPARG102;

The sequence of this isoform differs from the canonical sequence as follows:
     1-82: Missing.
Isoform 3 (identifier: Q86W56-3)

Also known as: hPARG99;

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.
Isoform 4 (identifier: Q86W56-4)

Also known as: hPARG60;

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MNAGPGCEPCTKRPR → MVQAGAEKDAQSISL
     16-423: Missing.
     485-526: RVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDE → W
Note: Catalytically inactive.
Isoform 5 (identifier: Q86W56-5)

Also known as: hPARG55;

The sequence of this isoform differs from the canonical sequence as follows:
     1-460: Missing.
     485-526: RVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDE → W
Note: Catalytically inactive.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 976976Poly(ADP-ribose) glycohydrolase
PRO_0000066602

Regions

Region1 – 456456A-domain
Region610 – 795186Catalytic
Region726 – 7272Substrate binding By similarity
Region869 – 8746Substrate binding By similarity
Motif10 – 167Nuclear localization signal Ref.2
Motif76 – 838PIP-box (PCNA interacting peptide)

Sites

Active site7371 By similarity
Active site7551 By similarity
Active site7561 By similarity
Binding site7401Substrate By similarity
Binding site7541Substrate; via amide nitrogen By similarity
Binding site7951Substrate By similarity

Amino acid modifications

Modified residue1331Phosphoserine Ref.10
Modified residue1371Phosphoserine Ref.10
Modified residue1971Phosphoserine Ref.10 Ref.11 Ref.12
Modified residue1991Phosphothreonine Ref.10 Ref.11 Ref.12
Modified residue2611Phosphoserine By similarity
Modified residue2641Phosphoserine By similarity
Modified residue2911Phosphoserine By similarity
Modified residue2981Phosphoserine Ref.11
Modified residue3021Phosphoserine Ref.16
Modified residue3401N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 460460Missing in isoform 5.
VSP_044674
Alternative sequence1 – 108108Missing in isoform 3.
VSP_011770
Alternative sequence1 – 8282Missing in isoform 2.
VSP_011769
Alternative sequence1 – 1515MNAGP…TKRPR → MVQAGAEKDAQSISL in isoform 4.
VSP_044675
Alternative sequence16 – 423408Missing in isoform 4.
VSP_044676
Alternative sequence485 – 52642RVDLL…PVEDE → W in isoform 4 and isoform 5.
VSP_044677

Experimental info

Mutagenesis121K → A: Abolishes nuclear targeting; when associated with G-13. Ref.2
Mutagenesis131R → G: Abolishes nuclear targeting; when associated with A-12. Ref.2
Mutagenesis361R → A: No effect. Ref.2
Mutagenesis371R → G: No effect. Ref.2
Sequence conflict13 – 142RP → AT in AAB61614. Ref.3
Sequence conflict611R → Q in AAB61614. Ref.3
Sequence conflict1271E → V in AAB61614. Ref.3
Sequence conflict1381P → L in AAB61614. Ref.3
Sequence conflict2271Q → H in AAB61614. Ref.3
Sequence conflict2421D → H in AAB61614. Ref.3
Sequence conflict2601E → K in AAB61614. Ref.3
Sequence conflict2751P → S in AAB61614. Ref.3
Sequence conflict2821T → I in AAB61614. Ref.3
Sequence conflict4141F → L in AAB61614. Ref.3
Sequence conflict4661R → Q in AFM56043. Ref.5
Sequence conflict4841I → V in AFM56043. Ref.5
Sequence conflict814 – 8152WQ → CE in AAB61614. Ref.3
Sequence conflict8171R → H in AAH52966. Ref.7

Secondary structure

............................................................................................ 976
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (hPARG111) [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: D6646353C6D0180E

FASTA976111,110
        10         20         30         40         50         60 
MNAGPGCEPC TKRPRWGAAT TSPAASDARS FPSRQRRVLD PKDAHVQFRV PPSSPACVPG 

        70         80         90        100        110        120 
RAGQHRGSAT SLVFKQKTIT SWMDTKGIKT AESESLDSKE NNNTRIESMM SSVQKDNFYQ 

       130        140        150        160        170        180 
HNVEKLENVS QLSLDKSPTE KSTQYLNQHQ TAAMCKWQNE GKHTEQLLES EPQTVTLVPE 

       190        200        210        220        230        240 
QFSNANIDRS PQNDDHSDTD SEENRDNQQF LTTVKLANAK QTTEDEQARE AKSHQKCSKS 

       250        260        270        280        290        300 
CDPGEDCASC QQDEIDVVPE SPLSDVGSED VGTGPKNDNK LTRQESCLGN SPPFEKESEP 

       310        320        330        340        350        360 
ESPMDVDNSK NSCQDSEADE ETSPGFDEQE DGSSSQTANK PSRFQARDAD IEFRKRYSTK 

       370        380        390        400        410        420 
GGEVRLHFQF EGGESRTGMN DLNAKLPGNI SSLNVECRNS KQHGKKDSKI TDHFMRLPKA 

       430        440        450        460        470        480 
EDRRKEQWET KHQRTERKIP KYVPPHLSPD KKWLGTPIEE MRRMPRCGIR LPLLRPSANH 

       490        500        510        520        530        540 
TVTIRVDLLR AGEVPKPFPT HYKDLWDNKH VKMPCSEQNL YPVEDENGER TAGSRWELIQ 

       550        560        570        580        590        600 
TALLNKFTRP QNLKDAILKY NVAYSKKWDF TALIDFWDKV LEEAEAQHLY QSILPDMVKI 

       610        620        630        640        650        660 
ALCLPNICTQ PIPLLKQKMN HSITMSQEQI ASLLANAFFC TFPRRNAKMK SEYSSYPDIN 

       670        680        690        700        710        720 
FNRLFEGRSS RKPEKLKTLF CYFRRVTEKK PTGLVTFTRQ SLEDFPEWER CEKPLTRLHV 

       730        740        750        760        770        780 
TYEGTIEENG QGMLQVDFAN RFVGGGVTSA GLVQEEIRFL INPELIISRL FTEVLDHNEC 

       790        800        810        820        830        840 
LIITGTEQYS EYTGYAETYR WSRSHEDGSE RDDWQRRCTE IVAIDALHFR RYLDQFVPEK 

       850        860        870        880        890        900 
MRRELNKAYC GFLRPGVSSE NLSAVATGNW GCGAFGGDAR LKALIQILAA AAAERDVVYF 

       910        920        930        940        950        960 
TFGDSELMRD IYSMHIFLTE RKLTVGDVYK LLLRYYNEEC RNCSTPGPDI KLYPFIYHAV 

       970 
ESCAETADHS GQRTGT 

« Hide

Isoform 2 (hPARG102) [UniParc].

Checksum: 666B77E891E4A500
Show »

FASTA894102,312
Isoform 3 (hPARG99) [UniParc].

Checksum: 85BCE7201ABABA5F
Show »

FASTA86899,432
Isoform 4 (hPARG60) [UniParc].

Checksum: 0FBB26152C56D33D
Show »

FASTA52760,873
Isoform 5 (hPARG55) [UniParc].

Checksum: 5443EFFA21AA84CE
Show »

FASTA47554,794

References

« Hide 'large scale' references
[1]"Human poly(ADP-ribose) glycohydrolase (PARG) gene and the common promoter sequence it shares with inner mitochondrial membrane translocase 23 (TIM23)."
Meyer R.G., Meyer-Ficca M.L., Jacobson E.L., Jacobson M.K.
Gene 314:181-190(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Skin.
[2]"Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments."
Meyer-Ficca M.L., Meyer R.G., Coyle D.L., Jacobson E.L., Jacobson M.K.
Exp. Cell Res. 297:521-532(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), MUTAGENESIS OF LYS-12; ARG-13; ARG-36 AND ARG-37, NUCLEAR LOCALIZATION SIGNAL.
Tissue: Skin.
[3]"Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to human chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization."
Ame J.-C., Apiou F., Jacobson E.L., Jacobson M.K.
Cytogenet. Cell Genet. 85:269-270(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Two small enzyme isoforms mediate mammalian mitochondrial poly(ADP-ribose) glycohydrolase (PARG) activity."
Meyer R.G., Meyer-Ficca M.L., Whatcott C.J., Jacobson E.L., Jacobson M.K.
Exp. Cell Res. 313:2920-2936(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), SUBCELLULAR LOCATION.
Tissue: Testis.
[5]"ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose)."
Niere M., Mashimo M., Agledal L., Dolle C., Kasamatsu A., Kato J., Moss J., Ziegler M.
J. Biol. Chem. 287:16088-16102(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING (ISOFORMS 4 AND 5), ABSENCE OF CATALYTIC ACTIVITY (ISOFORMS 4 AND 5), SUBCELLULAR LOCATION.
Tissue: Peripheral blood monocyte.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Brain cortex, Hippocampus and Testis.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Skin and Testis.
[8]"Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during radiation-induced DNA damage."
Haince J.F., Ouellet M.E., McDonald D., Hendzel M.J., Poirier G.G.
Biochim. Biophys. Acta 1763:226-237(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION (ISOFORMS 1 AND 2).
[9]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-137; SER-197 AND THR-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Proteomic investigation of phosphorylation sites in poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase."
Gagne J.P., Moreel X., Gagne P., Labelle Y., Droit A., Chevalier-Pare M., Bourassa S., McDonald D., Hendzel M.J., Prigent C., Poirier G.G.
J. Proteome Res. 8:1014-1029(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-197; THR-199 AND SER-298.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND THR-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"PARG is recruited to DNA damage sites through poly(ADP-ribose)- and PCNA-dependent mechanisms."
Mortusewicz O., Fouquerel E., Ame J.C., Leonhardt H., Schreiber V.
Nucleic Acids Res. 39:5045-5056(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION (ISOFORM 1), INTERACTION WITH PCNA.
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Poly (ADP-ribose) glycohydrolase regulates retinoic acid receptor-mediated gene expression."
Le May N., Iltis I., Ame J.C., Zhovmer A., Biard D., Egly J.M., Schreiber V., Coin F.
Mol. Cell 48:785-798(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY258587 mRNA. Translation: AAP83314.1.
AY575848 mRNA. Translation: AAT66421.1.
AY575849 mRNA. Translation: AAT66422.1.
AF005043 mRNA. Translation: AAB61614.1.
EF382674 mRNA. Translation: ABR10027.1.
JQ890226 mRNA. Translation: AFM56043.1.
AK295786 mRNA. Translation: BAG58607.1.
AK302560 mRNA. Translation: BAG63826.1.
AK314909 mRNA. Translation: BAG37421.1.
BC050560 mRNA. Translation: AAH50560.1.
BC052966 mRNA. Translation: AAH52966.1.
RefSeqNP_003622.2. NM_003631.2. [Q86W56-1]
UniGeneHs.10136.
Hs.535298.
Hs.732225.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4A0DX-ray1.75A448-976[»]
4B1GX-ray1.83A448-976[»]
4B1HX-ray2.00A448-976[»]
4B1IX-ray2.14A448-976[»]
4B1JX-ray2.08A448-976[»]
ProteinModelPortalQ86W56.
SMRQ86W56. Positions 450-963.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114077. 3 interactions.
IntActQ86W56. 1 interaction.
STRING9606.ENSP00000384408.

Chemistry

BindingDBQ86W56.
ChEMBLCHEMBL1795143.

PTM databases

PhosphoSiteQ86W56.

Polymorphism databases

DMDM56417893.

Proteomic databases

MaxQBQ86W56.
PaxDbQ86W56.
PRIDEQ86W56.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000402038; ENSP00000384408; ENSG00000227345.
GeneID8505.
KEGGhsa:8505.
UCSCuc001jif.3. human. [Q86W56-1]
uc010qgx.2. human. [Q86W56-3]

Organism-specific databases

CTD8505.
GeneCardsGC10M051026.
H-InvDBHIX0127080.
HGNCHGNC:8605. PARG.
HPAHPA021819.
MIM603501. gene.
neXtProtNX_Q86W56.
PharmGKBPA32940.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG254589.
HOVERGENHBG053510.
InParanoidQ86W56.
KOK07759.
PhylomeDBQ86W56.
TreeFamTF323527.

Gene expression databases

ArrayExpressQ86W56.
BgeeQ86W56.
CleanExHS_PARG.
GenevestigatorQ86W56.

Family and domain databases

InterProIPR007724. Poly_GlycHdrlase.
[Graphical view]
PANTHERPTHR12837. PTHR12837. 1 hit.
PfamPF05028. PARG_cat. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPARG. human.
GeneWikiPARG.
GenomeRNAi8505.
NextBio31829.
PMAP-CutDBQ86W56.
PROQ86W56.
SOURCESearch...

Entry information

Entry namePARG_HUMAN
AccessionPrimary (citable) accession number: Q86W56
Secondary accession number(s): A5YBK3 expand/collapse secondary AC list , B2RC24, B4DIU5, B4DYR4, I6RUV3, Q6E4P6, Q6E4P7, Q7Z742, Q9Y4W7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries